4mt5: Difference between revisions

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-'''Unreleased structure'''
+==Crystal structure of Mub-RV==
+<StructureSection load='4mt5' size='340' side='right' caption='[[4mt5]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[4mt5]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4MT5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4MT5 FirstGlance]. <br>
+</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3i57|3i57]]</td></tr>
+<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4mt5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mt5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4mt5 RCSB], [http://www.ebi.ac.uk/pdbsum/4mt5 PDBsum]</span></td></tr>
+<table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The mucus layer covering the gastrointestinal (GI) epithelium is critical in selecting and maintaining homeostatic interactions with our gut bacteria. However, the underpinning mechanisms of these interactions are not understood. Here, we provide structural and functional insights into the canonical mucus-binding protein (MUB), a multi-repeat cell-surface adhesin found in Lactobacillus inhabitants of the GI tract. X-ray crystallography together with small-angle X-ray scattering demonstrated a 'beads on a string' arrangement of repeats, generating 174 nm long protein fibrils, as shown by atomic force microscopy. Each repeat consists of tandemly arranged Ig- and mucin-binding protein (MucBP) modules. The binding of full-length MUB was confined to mucus via multiple interactions involving terminal sialylated mucin glycans. While individual MUB domains showed structural similarity to fimbrial proteins from Gram-positive pathogens, the particular organization of MUB provides a structural explanation for the mechanisms in which lactobacilli have adapted to their host niche by maximizing interactions with the mucus receptors, potentiating the retention of bacteria within the mucus layer. Together, this study reveals functional and structural features which may affect tropism of microbes across mucus and along the GI tract, providing unique insights into the mechanisms adopted by commensals and probiotics to adapt to the mucosal environment.
-The entry 4mt5 is ON HOLD  until Paper Publication
+Structural basis for adaptation of lactobacilli to gastrointestinal mucus.,Etzold S, Kober OI, Mackenzie DA, Tailford LE, Gunning AP, Walshaw J, Hemmings AM, Juge N Environ Microbiol. 2014 Mar;16(3):888-903. doi: 10.1111/1462-2920.12377. Epub, 2014 Jan 23. PMID:24373178<ref>PMID:24373178</ref>
-Authors: Etzold, S., Juge, N., Hemmings, A.M.
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
-Description: Crystal structure of Mub-RV
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Etzold, S.]]
+[[Category: Hemmings, A M.]]
+[[Category: Juge, N.]]
+[[Category: Cell-surface]]
+[[Category: Mucin binding]]
+[[Category: Protein binding]]
+[[Category: Ubiquitin-like beta-grasp fold]]